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Updated: Jul 19, 2026

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
Published on: August 20, 2018
A short water-soluble self-assembling peptide forms amyloid-like fibrils
Sudipta Ray1, Apurba K Das, Michael G B Drew
1Department of Biological Chemistry, Indian Association for the Cultivation of Science, Jadavpur, Kolkata, India.
Abstract:
A water-soluble tripeptide Val-Ile-Ala (VIA) , bearing sequence identity with the C-terminal portion of the Alzheimer Abeta-peptide (Abeta(40-42)), self-assembles, in crystalline form, to produce an intermolecularly hydrogen bonded supramolecular beta-sheet structure which self-associates to form straight, unbranched nanofibrils exhibiting amyloid-like behavior; in contrast, the synthetic tripeptide Ala-Val-Ile (AVI) self-assembles to produce a beta-sheet structure that forms branched nanofibrils which do not show any characteristic features of amyloid-like fibrils.
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